RADA_SULTO
ID RADA_SULTO Reviewed; 324 AA.
AC Q975Y1;
DT 05-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA repair and recombination protein RadA {ECO:0000255|HAMAP-Rule:MF_00348};
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_00348}; OrderedLocusNames=STK_02970;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
CC -!- FUNCTION: Involved in DNA repair and in homologous recombination. Binds
CC and assemble on single-stranded DNA to form a nucleoprotein filament.
CC Hydrolyzes ATP in a ssDNA-dependent manner and promotes DNA strand
CC exchange between homologous DNA molecules. {ECO:0000255|HAMAP-
CC Rule:MF_00348}.
CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family.
CC {ECO:0000255|HAMAP-Rule:MF_00348}.
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DR EMBL; BA000023; BAB65267.1; -; Genomic_DNA.
DR AlphaFoldDB; Q975Y1; -.
DR SMR; Q975Y1; -.
DR STRING; 273063.STK_02970; -.
DR EnsemblBacteria; BAB65267; BAB65267; STK_02970.
DR KEGG; sto:STK_02970; -.
DR PATRIC; fig|273063.9.peg.351; -.
DR eggNOG; arCOG00415; Archaea.
DR OMA; TFRIYLR; -.
DR BRENDA; 3.6.4.B7; 15396.
DR Proteomes; UP000001015; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR CDD; cd01123; Rad51_DMC1_radA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00348; RadA_arch; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C.
DR InterPro; IPR011938; DNA_recomb/repair_RadA.
DR InterPro; IPR016467; DNA_recomb/repair_RecA-like.
DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR033925; Rad51_DMC1_RadA.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR Pfam; PF08423; Rad51; 1.
DR PIRSF; PIRSF005856; Rad51; 1.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF47794; SSF47794; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR02236; recomb_radA; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 3: Inferred from homology;
KW ATP-binding; DNA damage; DNA recombination; DNA-binding;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..324
FT /note="DNA repair and recombination protein RadA"
FT /id="PRO_0000150108"
FT BINDING 114..121
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00348"
SQ SEQUENCE 324 AA; 35530 MW; 9F960973260B5CA1 CRC64;
MNDMSSDGKK VKSLSDLPGV GQSILNKLIE AGYSSLEAVA VASPQDLSVA AGIPLTTAQR
IIKEAREALD IRFKTALEVK KERINTKKIT TGSQALDGLL GGGIETRTMT ELFGEFGSGK
TQLCHQLSVN VQLPLEKGGL GGKAVYIDTE GTFRWERIEA MSKAIGLEPD SAMNNIYYMR
AINSDHQMAI VDDLQELISK DPAIKLVIVD SVTSHFRAEF PGRENLAVRQ QKLNKHLHQL
VRLAEMYDLA VIITNQVMAR PDMFYGDPTV AVGGHTLYHV PGIRVQLKKS RGNKRIARIV
DAPHLPEGEV VFAITEEGVR DAEE